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Potassium in PDB 3fwf: Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form

Enzymatic activity of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form

All present enzymatic activity of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form:
1.14.15.1;

Protein crystallography data

The structure of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form, PDB code: 3fwf was solved by I.Schlichting, K.Von Koenig, C.Aldag, D.Hilvert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.64 / 1.83
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.520, 61.930, 94.460, 90.00, 90.80, 90.00
R / Rfree (%) 16.2 / 20.7

Other elements in 3fwf:

The structure of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form (pdb code 3fwf). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form, PDB code: 3fwf:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 3fwf

Go back to Potassium Binding Sites List in 3fwf
Potassium binding site 1 out of 4 in the Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K515

b:16.5
occ:1.00
 O A:TYR96 2.6 15.3 1.0
O A:GLU84 2.7 17.4 1.0
O A:GLY93 2.8 16.0 1.0
O A:HOH430 2.8 25.9 1.0
O A:HOH467 2.9 35.8 1.0
O A:GLU94 2.9 18.4 1.0
C A:GLU94 3.5 17.5 1.0
C A:TYR96 3.7 15.4 1.0
C A:GLU84 3.8 17.4 1.0
CA A:GLU94 3.8 18.2 1.0
O A:HOH468 3.8 35.2 1.0
C A:GLY93 3.9 17.0 1.0
SG A:CYS85 3.9 27.0 0.5
N A:TYR96 4.1 16.1 1.0
CG A:GLU84 4.2 21.2 1.0
N A:GLU94 4.3 17.4 1.0
CA A:TYR96 4.4 14.8 1.0
CA A:CYS85 4.4 17.1 0.5
CA A:CYS85 4.4 19.5 0.5
N A:CYS85 4.5 18.2 0.5
N A:ALA95 4.5 16.8 1.0
N A:CYS85 4.5 17.1 0.5
C A:ALA95 4.5 16.0 1.0
CB A:TYR96 4.6 15.4 1.0
O A:HOH698 4.7 34.8 1.0
OE2 A:GLU84 4.7 24.9 1.0
N A:ASP97 4.8 13.5 1.0
CA A:GLU84 4.8 17.2 1.0
CB A:CYS85 4.8 19.6 0.5
CB A:CYS85 4.8 16.6 0.5
O A:HOH466 4.9 47.3 1.0
CA A:ASP97 5.0 14.8 1.0

Potassium binding site 2 out of 4 in 3fwf

Go back to Potassium Binding Sites List in 3fwf
Potassium binding site 2 out of 4 in the Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K515

b:11.8
occ:1.00
 O B:GLU84 2.6 13.2 1.0
O B:TYR96 2.6 11.5 1.0
O B:HOH519 2.8 24.0 1.0
O B:GLY93 2.8 14.0 1.0
O B:GLU94 2.8 11.8 1.0
O B:HOH467 3.2 34.5 1.0
C B:GLU94 3.5 12.2 1.0
C B:TYR96 3.7 10.9 1.0
CA B:GLU94 3.8 12.4 1.0
C B:GLU84 3.8 13.3 1.0
C B:GLY93 3.9 12.9 1.0
SG B:CYS85 3.9 25.6 0.5
N B:TYR96 4.1 11.8 1.0
O B:HOH530 4.3 37.4 1.0
N B:GLU94 4.3 12.2 1.0
O B:HOH537 4.4 37.2 1.0
CA B:TYR96 4.4 10.5 1.0
CA B:CYS85 4.4 11.4 0.5
CG B:GLU84 4.4 24.2 1.0
CA B:CYS85 4.5 15.1 0.5
C B:ALA95 4.5 13.0 1.0
N B:ALA95 4.5 12.0 1.0
N B:CYS85 4.5 13.7 0.5
N B:CYS85 4.5 12.0 0.5
CB B:TYR96 4.6 10.4 1.0
N B:ASP97 4.8 9.9 1.0
CA B:GLU84 4.8 13.6 1.0
CB B:CYS85 4.9 15.0 0.5
CB B:CYS85 4.9 10.4 0.5
O B:ALA95 4.9 12.1 1.0
CA B:ALA95 5.0 12.5 1.0
CA B:ASP97 5.0 11.1 1.0

Potassium binding site 3 out of 4 in 3fwf

Go back to Potassium Binding Sites List in 3fwf
Potassium binding site 3 out of 4 in the Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K715

b:16.3
occ:1.00
 O B:VAL18 2.6 13.8 1.0
O B:PRO16 2.8 15.8 1.0
O B:HOH8 2.8 17.2 1.0
OE2 B:GLU20 2.9 17.2 1.0
O B:PRO15 2.9 13.9 1.0
C B:PRO16 3.4 14.6 1.0
C B:VAL18 3.6 13.0 1.0
CD B:GLU20 3.6 18.8 1.0
CA B:PRO16 3.7 14.6 1.0
CD2 B:LEU14 3.7 16.9 1.0
C B:PRO15 3.9 14.7 1.0
N B:VAL18 3.9 12.0 1.0
OE1 B:GLU20 3.9 18.5 1.0
CG B:LEU14 4.0 15.6 1.0
O B:HOH425 4.1 25.2 1.0
N B:PRO16 4.2 15.0 1.0
CA B:VAL18 4.3 12.2 1.0
N B:HIS17 4.3 13.2 1.0
O B:HOH721 4.6 39.0 1.0
C B:HIS17 4.6 12.1 1.0
N B:PRO19 4.6 14.0 1.0
N B:GLU20 4.7 14.1 1.0
O B:LEU14 4.8 14.0 1.0
CA B:PRO19 4.8 14.1 1.0
CB B:VAL18 4.8 11.7 1.0
CG B:GLU20 4.8 16.4 1.0
CA B:HIS17 4.9 12.8 1.0
CB B:LEU14 4.9 14.3 1.0
C B:PRO19 5.0 14.3 1.0

Potassium binding site 4 out of 4 in 3fwf

Go back to Potassium Binding Sites List in 3fwf
Potassium binding site 4 out of 4 in the Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Ferric Camphor Bound Cytochrome P450CAM Containing A Selenocysteine As the 5TH Heme Ligand, Monoclinic Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K716

b:24.7
occ:1.00
 O B:HOH541 2.8 20.8 1.0
N B:ARG109 3.1 14.4 1.0
NH1 B:ARG109 3.2 18.8 1.0
C B:PRO106 3.4 17.8 1.0
O B:HOH540 3.4 19.9 1.0
CG B:ARG109 3.5 17.8 1.0
CA B:PRO106 3.5 17.6 1.0
CB B:ARG109 3.6 16.9 1.0
CA B:PRO105 3.6 15.3 1.0
O B:PRO106 3.6 18.4 1.0
N B:GLN108 3.7 14.3 1.0
N B:GLU107 3.9 16.8 0.5
CD B:ARG109 3.9 19.2 1.0
CA B:ARG109 3.9 15.5 1.0
CB B:PRO105 3.9 15.9 1.0
N B:GLU107 3.9 16.7 0.5
C B:GLN108 4.1 13.4 1.0
CZ B:ARG109 4.2 18.1 1.0
CA B:GLN108 4.2 13.3 1.0
CG B:PRO105 4.3 14.7 1.0
C B:GLU107 4.3 15.3 0.5
NE B:ARG109 4.4 16.6 1.0
C B:GLU107 4.4 15.5 0.5
CB B:GLN108 4.4 12.8 1.0
N B:PRO106 4.4 17.8 1.0
N B:PRO105 4.5 14.5 1.0
CA B:GLU107 4.5 16.3 0.5
C B:PRO105 4.6 16.8 1.0
CA B:GLU107 4.6 16.5 0.5
CB B:PRO106 4.6 17.0 1.0
OE1 B:GLN108 4.7 15.7 1.0
N B:GLN110 4.8 14.1 1.0
C B:ARG109 4.9 14.9 1.0
CD B:PRO105 5.0 14.4 1.0

Reference:

C.Aldag, I.A.Gromov, I.Garcia-Rubio, K.Von Koenig, I.Schlichting, B.Jaun, D.Hilvert. Probing the Role of the Proximal Heme Ligand in Cytochrome P450CAM By Recombinant Incorporation of Selenocysteine. Proc.Natl.Acad.Sci.Usa V. 106 5481 2009.
ISSN: ISSN 0027-8424
PubMed: 19293375
DOI: 10.1073/PNAS.0810503106
Page generated: Mon Aug 12 08:20:37 2024

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